The affinity antibody purification combined with LC MS/MS was used to investigate the lysine succinylome profile of A. hydrophila ATCC7966. A total of 666 lysine succinylation proteins were identified and analyzed in depth to better understand its regulatory roles. Lysine succinylation modifications on S-ribosylhomocysteine lyase were further studied and shown to regulate its cellular physiology and affect bacterial quorum sensing behavior of A. hydrophila.

Changes in proteome and phosphoproteome have been determined in E. coli treated with the antibiotics colistin or ciprofloxacin and in a bona-fide mcr-1 positive colistin resistant strain. The results reveal extensive phosphorylation on bacterial proteins and motif specific phosphorylation changes during resistance development. Moreover, regulated sites show high evolutionary conservation, indicating an important biological role. Together, this indicates that phosphorylation mediated signaling could be used as a specific target for drug design.